@article{
 title = {Alzheimer's disease-related protein hGas7b interferes with kinesin motility},
 type = {article},
 year = {2012},
 identifiers = {[object Object]},
 keywords = {cryo-EM,hGas7b,kinesin,microtubule,motility},
 volume = {151},
 id = {11953569-c0e4-36b3-bc59-2fac908903e8},
 created = {2018-02-28T22:42:48.334Z},
 file_attached = {false},
 profile_id = {a39b8b7f-45f4-3d11-94d2-dbc38be2487d},
 last_modified = {2018-02-28T22:42:48.334Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {false},
 hidden = {false},
 private_publication = {true},
 abstract = {In the previous study, we reported the important properties of hGas7b (i) that binds to phospho-tau and facilitates microtubule polymerization and (ii) the level of hGas7b is very low in the brains of patients with Alzheimer's disease. These results led us to study the function of hGas7b in detail. We focused on the effect of hGas7b on microtubule dynamics in the absence of tau, on the assumption of healthy tau decrease in the brains of Alzheimer's disease. hGas7b binds to microtubule directly without tau, although this binding does not enhance microtubule polymerization. Excess hGas7b interferes with kinesin motility on microtubules. These results suggest that regulation to maintain an appropriate concentration of hGas7b is required for healthy neurotransmission. © 2012 The Authors. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.},
 bibtype = {article},
 author = {Hidaka, M. and Koga, T. and Gotoh, A. and Sanada, M. and Hirose, K. and Uchida, T.},
 journal = {Journal of Biochemistry},
 number = {6}
}

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